Header list of 1yuj.pdb file
Complete list - r 2 2 Bytes
HEADER DNA BINDING PROTEIN/DNA 31-DEC-96 1YUJ
TITLE SOLUTION NMR STRUCTURE OF THE GAGA FACTOR/DNA COMPLEX, 50 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA (5'-D(*GP*CP*CP*GP*AP*GP*AP*GP*TP*AP*C)-3');
COMPND 3 CHAIN: B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: DNA (5'-D(*GP*TP*AP*CP*TP*CP*TP*CP*GP*GP*C)-3');
COMPND 7 CHAIN: C;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: GAGA-FACTOR;
COMPND 11 CHAIN: A;
COMPND 12 FRAGMENT: DNA BINDING DOMAIN, RESIDUES 310 - 372
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 MOL_ID: 2;
SOURCE 4 SYNTHETIC: YES;
SOURCE 5 MOL_ID: 3;
SOURCE 6 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;
SOURCE 7 ORGANISM_COMMON: FRUIT FLY;
SOURCE 8 ORGANISM_TAXID: 7227
KEYWDS COMPLEX (DNA-BINDING PROTEIN-DNA), CHROMATIN REMODELING, DNA BINDING
KEYWDS 2 PROTEIN-DNA COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 50
AUTHOR G.M.CLORE,J.G.OMICHINSKI,A.M.GRONENBORN
REVDAT 3 02-MAR-22 1YUJ 1 REMARK LINK
REVDAT 2 24-FEB-09 1YUJ 1 VERSN
REVDAT 1 31-DEC-97 1YUJ 0
JRNL AUTH J.G.OMICHINSKI,P.V.PEDONE,G.FELSENFELD,A.M.GRONENBORN,
JRNL AUTH 2 G.M.CLORE
JRNL TITL THE SOLUTION STRUCTURE OF A SPECIFIC GAGA FACTOR-DNA COMPLEX
JRNL TITL 2 REVEALS A MODULAR BINDING MODE.
JRNL REF NAT.STRUCT.BIOL. V. 4 122 1997
JRNL REFN ISSN 1072-8368
JRNL PMID 9033593
JRNL DOI 10.1038/NSB0297-122
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER (X-PLOR (SEE ABOVE) ABOVE)), BRUNGER (X
REMARK 3 -PLOR (SEE ABOVE) ABOVE))
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE 3D STRUCTURE OF THE GAGA FACTOR/DNA COMPLEX WAS SOLVED
REMARK 3 BY MULTI-DIMENSIONAL HETERONUCLEAR-EDITED AND -FILTERED
REMARK 3 NMR AND IS BASED ON 1475 EXPERIMENTAL NMR RESTRAINTS:
REMARK 3 (A) INTRAPROTEIN: 188 SEQUENTIAL (|I- J|=1), 134 MEDIUM
REMARK 3 RANGE (1 < |I-J| <=5) AND 95 LONG RANGE (|I-J| >5)
REMARK 3 INTERRESIDUES AND 275 INTRARESIDUE APPROXIMATE INTERPROTON
REMARK 3 DISTANCE RESTRAINTS; 140 TORSION ANGLE RESTRAINTS; 33
REMARK 3 THREE-BOND HN-HA COUPLING CONSTANT RESTRAINTS; AND 94
REMARK 3 (48 CALPHA AND 46 CBETA) 13C SHIFT RESTRAINTS. (NUMBERS
REMARK 3 OF RESIDUES 10 - 61)
REMARK 3 (B) INTRA-DNA: 124 INTRARESIDUE, 112 SEQUENTIAL
REMARK 3 INTRASTRAND, 21 INTERSTRAND INTERPROTON DISTANCE
REMARK 3 RESTRAINTS; 102 TORSION ANGLE RESTRAINTS (FOR ALPHA, BETA,
REMARK 3 GAMMA, DELTA, EPSILON AND AND ZETA BACKBONE TORSION
REMARK 3 ANGLES).
REMARK 3 (C) INTERMOLECULAR: 75 INTERPROTON DISTANCE RESTRAINTS.
REMARK 3 THE EXPERIMENTAL NMR RESTRAINTS ARE SUPPLEMENTED BY
REMARK 3 HYDROGEN BONDING RESTRAINTS: 24 DISTANCES FOR 12 BACKBONE
REMARK 3 HYDROGEN BONDS WITHIN THE PROTEIN, 58 DISTANCES FOR
REMARK 3 WATSON-CRICK BASE-PAIRING WITHIN THE DNA, AND 10 AMBIGUOUS
REMARK 3 DISTANCE RESTRAINTS BETWEEN THE PROTEIN AND THE DNA. THE
REMARK 3 RESTRAINTS HAVE BEEN DEPOSITED.
REMARK 3
REMARK 3 THE STRUCTURES WERE CALCULATED USING THE SIMULATED
REMARK 3 ANNEALING PROTOCOL OF NILGES ET AL. (1988) FEBS LETT. 229,
REMARK 3 129-136 USING THE PROGRAM X-PLOR 3.1 (BRUNGER) MODIFIED
REMARK 3 TO INCORPORATE COUPLING CONSTANT (GARRETT ET AL. (1984) J.
REMARK 3 MAGN. RESON. SERIES B 104, 99-103) AND CARBON CHEMICAL
REMARK 3 SHIFT (KUSZEWSKI ET AL. (1995) J. MAGN. RESON. SERIES B
REMARK 3 106, 92-96) RESTRAINTS, AND A CONFORMATIONAL DATABASE
REMARK 3 POTENTIAL (KUSZEWSKI ET AL.(1996) PROTEIN SCI. 5, 1067-1080
REMARK 3
REMARK 3 THE RESTRAINED REGULARIZED MEAN STRUCTURE IS PRESENTED IN
REMARK 3 ENTRY 1YUI AND 50 STRUCTURES ARE PRESENTED IN THIS ENTRY.
REMARK 3 IN THE RESTRAINED REGULARIZED MEAN COORDINATES THE LAST
REMARK 3 COLUMN REPRESENTS THE AVERAGE RMS DIFFERENCE BETWEEN THE
REMARK 3 INDIVIDUAL SIMULATED ANNEALING STRUCTURES AND THE MEAN
REMARK 3 COORDINATE POSITIONS. THE LAST COLUMN IN THE INDIVIDUAL SA
REMARK 3 STRUCTURES HAS NO MEANING. BEST FITTING TO GENERATE THE
REMARK 3 AVERAGE STRUCTURE IS WITH RESPECT TO RESIDUES 14 - 58 OF
REMARK 3 THE PROTEIN AND BASE PAIRS 1 - 11 OF THE DNA (RESIDUES 10 -
REMARK 3 13 AND 59 - 61 ARE DISORDERED IN SOLUTION). RESIDUE 10
REMARK 3 CORRESPONDS TO RESIDUE 319 OF THE NATURAL SEQUENCE. NOTE
REMARK 3 THE OCCUPANCY FIELD HAS NO MEANING.
REMARK 4
REMARK 4 1YUJ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000177449.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303.50
REMARK 210 PH : 6.00
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : TRIPLE RESONANCE
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : AMX500; AMX600
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 50
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: TRIPLE RESONANCE FOR ASSIGNMENT OF PROTEIN 12C- FILTERED
REMARK 210 NOE, 12C-FILTERED HOHAHA AND 1H-1H NOE FOR DNA. QUANTITATIVE J
REMARK 210 CORRELATION FOR COUPLING CONSTANTS 3D 15N- SEPARATED, 3D 13C-
REMARK 210 SEPARATED, 3D 12C-FILTERED 3D 13C- SEPARATED/12C-FILTERED, AND
REMARK 210 2D 1H-1H NOE EXPERIMENTS.
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C, A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 1 DT C 113 C5 DT C 113 C7 0.037
REMARK 500 3 DT C 118 C5 DT C 118 C7 0.038
REMARK 500 4 DT B 109 C5 DT B 109 C7 0.036
REMARK 500 5 DT C 118 C5 DT C 118 C7 0.040
REMARK 500 7 DT C 118 C5 DT C 118 C7 0.037
REMARK 500 8 DT C 118 C5 DT C 118 C7 0.037
REMARK 500 9 DT C 118 C5 DT C 118 C7 0.038
REMARK 500 10 DT C 113 C5 DT C 113 C7 0.039
REMARK 500 10 DT C 116 C5 DT C 116 C7 0.037
REMARK 500 12 DT C 118 C5 DT C 118 C7 0.038
REMARK 500 13 DT B 109 C5 DT B 109 C7 0.038
REMARK 500 13 DT C 118 C5 DT C 118 C7 0.036
REMARK 500 15 DT C 113 C5 DT C 113 C7 0.038
REMARK 500 16 DT C 118 C5 DT C 118 C7 0.037
REMARK 500 18 DT C 118 C5 DT C 118 C7 0.036
REMARK 500 19 DT C 118 C5 DT C 118 C7 0.038
REMARK 500 22 DT C 116 C5 DT C 116 C7 0.039
REMARK 500 24 DT C 113 C5 DT C 113 C7 0.036
REMARK 500 26 DT C 118 C5 DT C 118 C7 0.038
REMARK 500 29 DT C 116 C5 DT C 116 C7 0.039
REMARK 500 30 DT C 116 C5 DT C 116 C7 0.037
REMARK 500 31 DT C 113 C5 DT C 113 C7 0.036
REMARK 500 33 DT C 116 C5 DT C 116 C7 0.037
REMARK 500 33 DT C 118 C5 DT C 118 C7 0.037
REMARK 500 36 DT C 116 C5 DT C 116 C7 0.036
REMARK 500 38 DT C 116 C5 DT C 116 C7 0.039
REMARK 500 40 DT C 113 C5 DT C 113 C7 0.038
REMARK 500 41 DT C 113 C5 DT C 113 C7 0.037
REMARK 500 41 DT C 116 C5 DT C 116 C7 0.039
REMARK 500 41 DT C 118 C5 DT C 118 C7 0.037
REMARK 500 44 DT C 118 C5 DT C 118 C7 0.042
REMARK 500 45 DT C 118 C5 DT C 118 C7 0.039
REMARK 500 46 DT C 113 C5 DT C 113 C7 0.038
REMARK 500 47 DT C 118 C5 DT C 118 C7 0.037
REMARK 500 48 DT C 116 C5 DT C 116 C7 0.037
REMARK 500 49 DT C 113 C5 DT C 113 C7 0.040
REMARK 500 49 DT C 116 C5 DT C 116 C7 0.039
REMARK 500 49 DT C 118 C5 DT C 118 C7 0.039
REMARK 500 50 DT C 113 C5 DT C 113 C7 0.037
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 1 DG B 101 O4' - C1' - N9 ANGL. DEV. = 2.2 DEGREES
REMARK 500 1 DC B 102 O4' - C1' - N1 ANGL. DEV. = 2.4 DEGREES
REMARK 500 1 DC B 103 O4' - C1' - N1 ANGL. DEV. = 2.0 DEGREES
REMARK 500 1 DG B 104 O4' - C1' - N9 ANGL. DEV. = 2.7 DEGREES
REMARK 500 1 DA B 105 O4' - C1' - N9 ANGL. DEV. = 2.6 DEGREES
REMARK 500 1 DA B 107 O4' - C1' - N9 ANGL. DEV. = 2.0 DEGREES
REMARK 500 1 DG B 108 O4' - C1' - N9 ANGL. DEV. = 3.1 DEGREES
REMARK 500 1 DT B 109 O4' - C1' - N1 ANGL. DEV. = 2.2 DEGREES
REMARK 500 1 DA B 110 O4' - C1' - N9 ANGL. DEV. = 1.9 DEGREES
REMARK 500 1 DC B 111 O4' - C1' - N1 ANGL. DEV. = 2.5 DEGREES
REMARK 500 1 DG C 112 O4' - C1' - N9 ANGL. DEV. = 2.8 DEGREES
REMARK 500 1 DT C 113 O4' - C1' - N1 ANGL. DEV. = 2.2 DEGREES
REMARK 500 1 DA C 114 O4' - C1' - N9 ANGL. DEV. = 3.0 DEGREES
REMARK 500 1 DT C 116 O4' - C1' - N1 ANGL. DEV. = 2.0 DEGREES
REMARK 500 1 DC C 117 O4' - C1' - N1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 1 DT C 118 O4' - C1' - N1 ANGL. DEV. = 2.6 DEGREES
REMARK 500 1 DC C 119 O4' - C1' - N1 ANGL. DEV. = 2.8 DEGREES
REMARK 500 1 DG C 120 O4' - C1' - N9 ANGL. DEV. = 3.1 DEGREES
REMARK 500 1 DG C 121 O4' - C1' - N9 ANGL. DEV. = 2.5 DEGREES
REMARK 500 1 DC C 122 O4' - C1' - N1 ANGL. DEV. = 2.4 DEGREES
REMARK 500 2 DG B 101 O4' - C1' - N9 ANGL. DEV. = 2.2 DEGREES
REMARK 500 2 DC B 102 O4' - C1' - N1 ANGL. DEV. = 2.3 DEGREES
REMARK 500 2 DC B 103 O4' - C1' - N1 ANGL. DEV. = 2.6 DEGREES
REMARK 500 2 DG B 104 O4' - C1' - N9 ANGL. DEV. = 2.5 DEGREES
REMARK 500 2 DA B 105 O4' - C1' - N9 ANGL. DEV. = 3.8 DEGREES
REMARK 500 2 DG B 106 O4' - C1' - N9 ANGL. DEV. = 1.8 DEGREES
REMARK 500 2 DA B 107 O4' - C1' - N9 ANGL. DEV. = 2.2 DEGREES
REMARK 500 2 DG B 108 O4' - C1' - N9 ANGL. DEV. = 3.5 DEGREES
REMARK 500 2 DT B 109 O4' - C1' - N1 ANGL. DEV. = 1.9 DEGREES
REMARK 500 2 DA B 110 O4' - C1' - N9 ANGL. DEV. = 2.1 DEGREES
REMARK 500 2 DC B 111 O4' - C1' - N1 ANGL. DEV. = 2.6 DEGREES
REMARK 500 2 DG C 112 O4' - C1' - N9 ANGL. DEV. = 2.8 DEGREES
REMARK 500 2 DT C 113 O4' - C1' - N1 ANGL. DEV. = 2.1 DEGREES
REMARK 500 2 DA C 114 O4' - C1' - N9 ANGL. DEV. = 1.8 DEGREES
REMARK 500 2 DT C 116 O4' - C1' - N1 ANGL. DEV. = 2.3 DEGREES
REMARK 500 2 DT C 116 C6 - C5 - C7 ANGL. DEV. = -3.8 DEGREES
REMARK 500 2 DC C 117 O4' - C1' - N1 ANGL. DEV. = 2.7 DEGREES
REMARK 500 2 DT C 118 O4' - C1' - N1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 2 DC C 119 O4' - C1' - N1 ANGL. DEV. = 2.2 DEGREES
REMARK 500 2 DG C 120 O4' - C1' - N9 ANGL. DEV. = 2.6 DEGREES
REMARK 500 2 DG C 121 O4' - C1' - N9 ANGL. DEV. = 2.2 DEGREES
REMARK 500 2 DC C 122 O4' - C1' - N1 ANGL. DEV. = 2.5 DEGREES
REMARK 500 3 DG B 101 O4' - C1' - N9 ANGL. DEV. = 2.2 DEGREES
REMARK 500 3 DC B 102 O4' - C1' - N1 ANGL. DEV. = 2.3 DEGREES
REMARK 500 3 DC B 103 O4' - C1' - N1 ANGL. DEV. = 2.5 DEGREES
REMARK 500 3 DG B 104 O4' - C1' - N9 ANGL. DEV. = 2.7 DEGREES
REMARK 500 3 DA B 105 O4' - C1' - N9 ANGL. DEV. = 3.1 DEGREES
REMARK 500 3 DG B 106 O4' - C1' - N9 ANGL. DEV. = 2.0 DEGREES
REMARK 500 3 DA B 107 O4' - C1' - N9 ANGL. DEV. = 2.5 DEGREES
REMARK 500 3 DG B 108 O4' - C1' - N9 ANGL. DEV. = 3.2 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 1037 ANGLE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 1 LYS A 23 76.61 -106.67
REMARK 500 1 PRO A 33 156.31 -38.93
REMARK 500 1 TYR A 40 19.98 55.30
REMARK 500 1 HIS A 57 -73.26 -150.90
REMARK 500 2 LYS A 11 -2.35 -151.86
REMARK 500 2 LYS A 13 -130.00 -80.35
REMARK 500 2 LYS A 23 74.03 -106.26
REMARK 500 2 PRO A 33 154.39 -39.79
REMARK 500 2 PRO A 37 -4.09 -54.49
REMARK 500 2 TYR A 40 19.17 55.31
REMARK 500 2 HIS A 57 -65.73 -145.64
REMARK 500 2 PRO A 61 155.35 -46.36
REMARK 500 3 ALA A 12 4.93 -158.49
REMARK 500 3 PRO A 19 177.95 -50.79
REMARK 500 3 LYS A 23 76.03 -107.07
REMARK 500 3 PRO A 33 154.62 -40.12
REMARK 500 3 PRO A 37 -4.59 -54.10
REMARK 500 3 HIS A 57 -60.06 -148.18
REMARK 500 4 LYS A 13 -73.99 -86.51
REMARK 500 4 LYS A 23 71.03 -104.44
REMARK 500 4 PRO A 33 152.72 -34.64
REMARK 500 4 TYR A 40 20.97 48.43
REMARK 500 4 HIS A 57 -69.26 -150.87
REMARK 500 5 PRO A 19 -178.53 -64.76
REMARK 500 5 LYS A 23 74.04 -106.90
REMARK 500 5 PRO A 33 156.31 -38.30
REMARK 500 5 PRO A 37 0.46 -56.30
REMARK 500 5 ILE A 38 -61.63 -97.72
REMARK 500 5 HIS A 57 -71.84 -150.76
REMARK 500 5 ALA A 59 16.76 -68.98
REMARK 500 6 ALA A 12 7.81 -159.75
REMARK 500 6 LYS A 23 71.05 -107.24
REMARK 500 6 SER A 26 1.61 -67.18
REMARK 500 6 ARG A 27 -65.15 -94.02
REMARK 500 6 HIS A 57 -70.30 -152.11
REMARK 500 7 PRO A 33 153.56 -44.52
REMARK 500 7 TYR A 40 20.14 46.50
REMARK 500 7 HIS A 57 -76.68 -153.50
REMARK 500 8 LYS A 11 -73.85 -82.31
REMARK 500 8 LYS A 13 -99.41 -88.67
REMARK 500 8 LYS A 23 70.77 -105.15
REMARK 500 8 PRO A 33 156.50 -40.28
REMARK 500 8 TYR A 40 17.92 49.89
REMARK 500 8 HIS A 57 -71.05 -152.49
REMARK 500 8 PRO A 61 163.92 -47.47
REMARK 500 9 ALA A 12 22.50 -155.74
REMARK 500 9 PRO A 18 150.95 -48.06
REMARK 500 9 PRO A 19 175.41 -57.30
REMARK 500 9 LYS A 23 68.99 -106.66
REMARK 500 9 PRO A 33 153.09 -48.45
REMARK 500
REMARK 500 THIS ENTRY HAS 282 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 64 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 36 SG
REMARK 620 2 CYS A 39 SG 107.2
REMARK 620 3 HIS A 52 NE2 106.5 107.5
REMARK 620 4 HIS A 57 NE2 106.7 122.8 105.1
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 64
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1YUI RELATED DB: PDB
REMARK 900 REGULARIZED MEAN STRUCTURE
DBREF 1YUJ A 10 63 UNP Q08605 GAGA_DROME 319 372
DBREF 1YUJ B 101 111 PDB 1YUJ 1YUJ 101 111
DBREF 1YUJ C 112 122 PDB 1YUJ 1YUJ 112 122
SEQRES 1 B 11 DG DC DC DG DA DG DA DG DT DA DC
SEQRES 1 C 11 DG DT DA DC DT DC DT DC DG DG DC
SEQRES 1 A 54 PRO LYS ALA LYS ARG ALA LYS HIS PRO PRO GLY THR GLU
SEQRES 2 A 54 LYS PRO ARG SER ARG SER GLN SER GLU GLN PRO ALA THR
SEQRES 3 A 54 CYS PRO ILE CYS TYR ALA VAL ILE ARG GLN SER ARG ASN
SEQRES 4 A 54 LEU ARG ARG HIS LEU GLU LEU ARG HIS PHE ALA LYS PRO
SEQRES 5 A 54 GLY VAL
HET ZN A 64 1
HETNAM ZN ZINC ION
FORMUL 4 ZN ZN 2+
HELIX 1 1 ARG A 25 SER A 28 1 4
HELIX 2 2 SER A 46 ARG A 56 1 11
SHEET 1 A 2 ALA A 34 THR A 35 0
SHEET 2 A 2 VAL A 42 ILE A 43 -1 N ILE A 43 O ALA A 34
LINK SG CYS A 36 ZN ZN A 64 1555 1555 2.31
LINK SG CYS A 39 ZN ZN A 64 1555 1555 2.31
LINK NE2 HIS A 52 ZN ZN A 64 1555 1555 2.01
LINK NE2 HIS A 57 ZN ZN A 64 1555 1555 2.00
SITE 1 AC1 4 CYS A 36 CYS A 39 HIS A 52 HIS A 57
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
Complete list - r 2 2 Bytes